Evidence map›Paper›PMID 36823138›Full record

ArticleNature communications2023

Evolution of enzyme functionality in the flavin-containing monooxygenases.

Gautier Bailleul, Guang Yang, Callum R Nicoll, Andrea Mattevi, Marco W Fraaije, Maria Laura Mascotti

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Surveying aIranian journal of microbiology · 2026
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  3. Review
  4. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  5. Article
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  8. Review
  9. Article
  10. UnveilingFrontiers in cellular and infection microbiology · 2025
    Article
  11. Analysis of the sulfate permease family inFrontiers in plant science · 2025
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Gautier Bailleul *Molecular Enzymology group, University of Groningen, Groningen, The Netherlands.ORCID 0000-0001-5083-2727
Guang Yang *Molecular Enzymology group, University of Groningen, Groningen, The Netherlands.ORCID 0000-0002-6143-238X
Callum R NicollDepartment of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, Pavia, Italy.
Andrea MatteviDepartment of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, Pavia, Italy.ORCID 0000-0002-9523-7128
Marco W FraaijeMolecular Enzymology group, University of Groningen, Groningen, The Netherlands.ORCID 0000-0001-6346-5014
Maria Laura MascottiMolecular Enzymology group, University of Groningen, Groningen, The Netherlands. m.l.mascotti@rug.nl.ORCID 0000-0002-5817-4631

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among the molecular mechanisms of adaptation in biology, enzyme functional diversification is indispensable. By allowing organisms to expand their catalytic repertoires and adopt fundamentally different chemistries, animals can harness or eliminate new-found substances and xenobiotics that they are exposed to in new environments. Here, we explore the flavin-containing monooxygenases (FMOs) that are essential for xenobiotic detoxification. Employing a paleobiochemistry approach in combination with enzymology techniques we disclose the set of historical substitutions responsible for the family's functional diversification in tetrapods. Remarkably, a few amino acid replacements differentiate an ancestral multi-tasking FMO into a more specialized monooxygenase by modulating the oxygenating flavin intermediate. Our findings substantiate an ongoing premise that enzymatic function hinges on a subset of residues that is not limited to the active site core.

Indexed as

Mixed Function OxygenasesOxygenasesAnimalsCatalysisFlavinsdimethylaniline monooxygenase (N-oxide forming)FlavinsMixed Function OxygenasesOxygenases

Identifiers

PMID36823138
PMCPMC9950137

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.